<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kuksin, Dmitry</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoplasm</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Assembly</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">86</style></volume><pages><style face="normal" font="default" size="100%">1555-62</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The nonenveloped polyomavirus simian virus 40 (SV40) is taken up into cells by a caveola-mediated endocytic process that delivers the virus to the endoplasmic reticulum (ER). Within the ER lumen, the capsid undergoes partial disassembly, which exposes its internal capsid proteins VP2 and VP3 to immunostaining with antibodies. We demonstrate here that the SV40 genome does not become accessible to detection while the virus is in the ER. Instead, the genome becomes accessible two distinct detection procedures, one using anti-bromodeoxyuridine antibodies and the other using a 5-ethynyl-2-deoxyuridine-based chemical reaction, only after the emergence of partially disassembled SV40 particles in the cytoplasm. These cytoplasmic particles retain some of the SV40 capsid proteins, VP1, VP2, and VP3, in addition to the viral genome. Thus, SV40 particles undergo discrete disassembly steps during entry that are separated temporally and topologically. First, a partial disassembly of the particles occurs in the ER, which exposes internal capsid proteins VP2 and VP3. Then, in the cytoplasm, disassembly progresses further to also make the genomic DNA accessible to immune detection.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22090139?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Daniels, Robert</style></author><author><style face="normal" font="default" size="100%">Rusan, Nasser M</style></author><author><style face="normal" font="default" size="100%">Wilbuer, Anne-Kathrin</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Wadsworth, Patricia</style></author><author><style face="normal" font="default" size="100%">Hebert, Daniel N</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsid Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Death</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane Permeability</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Envelope</style></keyword><keyword><style  face="normal" font="default" size="100%">Permeability</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">80</style></volume><pages><style face="normal" font="default" size="100%">6575-87</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Many nonenveloped viruses have evolved an infectious cycle that culminates in the lysis or permeabilization of the host to enable viral release. How these viruses initiate the lytic event is largely unknown. Here, we demonstrated that the simian virus 40 progeny accumulated at the nuclear envelope prior to the permeabilization of the nuclear, endoplasmic reticulum, and plasma membranes at a time which corresponded with the release of the progeny. The permeabilization of these cellular membranes temporally correlated with late protein expression and was not observed upon the inhibition of their synthesis. To address whether one or more of the late proteins possessed an inherent capacity to induce membrane permeabilization, we examined the permeability of Escherichia coli that separately expressed the late proteins. VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes. Additionally, VP3 expression resulted in bacterial cell lysis. These findings demonstrate that VP3 possesses an inherent lytic property that is independent of eukaryotic signaling or cell death pathways.</style></abstract><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16775344?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Kuksin, Dmitry</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The caveolae-mediated sv40 entry pathway bypasses the golgi complex en route to the endoplasmic reticulum.</style></title><secondary-title><style face="normal" font="default" size="100%">Virol J</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Virol. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibroblasts</style></keyword><keyword><style  face="normal" font="default" size="100%">Golgi Apparatus</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunohistochemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2005</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">2</style></volume><pages><style face="normal" font="default" size="100%">38</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: Simian virus 40 (SV40) enters cells via an atypical caveolae-mediated endocytic pathway, which delivers the virus to a new intermediary compartment, the caveosome. The virus then is believed to go directly from the caveosome to the endoplasmic reticulum. Cholera toxin likewise enters via caveolae and traffics to caveosomes. But, in contrast to SV40, cholera toxin is transported from caveosomes to the endoplasmic reticulum via the Golgi. For that reason, and because the caveosome and Golgi may have some common markers, we revisited the issue of whether SV40 might access the endoplasmic reticulum via the Golgi.

RESULTS: We confirmed our earlier finding that SV40 co localizes with the Golgi marker beta-COP. However, we show that the virus does not co localize with the more discriminating Golgi markers, golgin 97 and BODIPY-ceramide.

CONCLUSION: The caveolae-mediated SV40 entry pathway does not intersect the Golgi. SV40 is seen to co localize with beta-COP because that protein is a marker for caveosomes as well as the Golgi. Moreover, these results are consistent with the likelihood that the caveosome is a sorting organelle. In addition, there are at least two distinct but related routes by which a ligand might traffic from the caveosome to the ER; one route involving transport through the Golgi, and another pathway that does not involve the Golgi.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15840166?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Anderson, Howard A</style></author><author><style face="normal" font="default" size="100%">Wolfrom, Scott A</style></author><author><style face="normal" font="default" size="100%">Oppenheim, Ariella</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antiviral Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Brefeldin A</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsid</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Coatomer Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">76</style></volume><pages><style face="normal" font="default" size="100%">5156-66</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) enters cells by atypical endocytosis mediated by caveolae that transports the virus to the endoplasmic reticulum (ER) instead of to the endosomal-lysosomal compartment, which is the usual destination for viruses and other cargo that enter by endocytosis. We show here that SV4O is transported to the ER via an intermediate compartment that contains beta-COP, which is best known as a component of the COPI coatamer complexes that are required for the retrograde retrieval pathway from the Golgi to the ER. Additionally, transport of SV40 to the ER, as well as infection, is sensitive to brefeldin A. This drug acts by specifically inhibiting the ARF1 GTPase, which is known to regulate assembly of COPI coat complexes on Golgi cisternae. Moreover, some beta-COP colocalizes with intracellular caveolin-1, which was previously shown to be present on a new organelle (termed the caveosome) that is an intermediate in the transport of SV40 to the ER (L. Pelkmans, J. Kartenbeck, and A. Helenius, Nat. Cell Biol. 3:473-483, 2001). We also show that the internal SV40 capsid proteins VP2 and VP3 become accessible to immunostaining starting at about 5 h. Most of that immunostaining overlays the ER, with some appearing outside of the ER. In contrast, immunostaining with anti-SV40 antisera remains confined to the ER.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11967331?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Exp Cell Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Exp. Cell Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Northern</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Cholesterol</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, myc</style></keyword><keyword><style  face="normal" font="default" size="100%">Genistein</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Octoxynol</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Solubility</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Jan 10</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">246</style></volume><pages><style face="normal" font="default" size="100%">83-90</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">It was reported earlier that entry of simian virus 40 (SV40) into cells is promoted by a signal transmitted by the virus from the cell surface and that SV40 enters cells through caveolae. It is shown here that bound SV40 begins to partition into a caveolae-enriched Triton X-100-insoluble membrane fraction at 30 min postadsorption. Maximal levels of SV40 were seen in that fraction at 1 h. The sterol-binding agent nystatin, which selectively disrupts the cholesterol-enriched caveolae-containing membrane microdomain, selectively blocked the SV40-induced signal. This implies that the SV40 signal is transmitted from that membrane microdomain. The tyrosine kinase inhibitor genistein, which was earlier shown to block the SV40-induced signal and infectious entry, did not block the partitioning of SV40 into the detergent-insoluble membrane fraction. This shows that the signal is not required for the translocation of SV40 to the detergent-insoluble membrane and is consistent with the finding that the signal is likely transmitted from that membrane microdomain. However, electron microscopy of the Triton X-100-insoluble membrane fraction showed that genistein caused SV40 particles to accumulate at the annuli or mouths of the caveolae. In contrast, most SV40 particles were found enclosed within caveolae in parallel samples from untreated control cells. Together, these results imply that SV40 initially binds to flat detergent-soluble membrane. The virus then translocates to a caveolae-containing detergent-insoluble membrane microdomain. From the flat portion of that membrane microdomain the virus induces a signal which promotes its entry into caveolae.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9882517?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Simian virus 40 infection via MHC class I molecules and caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Immunol Rev</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Immunol. Rev.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Papillomavirus Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Tumor Virus Infections</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">168</style></volume><pages><style face="normal" font="default" size="100%">13-22</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MHC class I molecules are a necessary component of the cell surface receptor for simian virus 40 (SV40). After binding to class I molecules, SV40 enters cells via a unique endocytic pathway that involves caveolae, rather than clathrin-coated pits. This pathway is dependent on a transmembrane signal that SV40 transmits from the cell surface. Furthermore, it delivers SV40 to the endoplasmic reticulum, rather than to the endosomal/lysosomal compartment, which is the usual target for endocytic traffic. The glycosphingolipid and cholesterol-enriched plasma membrane domains that contain caveolae are also enriched for class I molecules, relative to whole plasma membrane. Nevertheless, although class I molecules bind SV40, they do not enter with SV40, nor do they enter spontaneously into uninfected SV40 host cells. Instead, they are shed from the cell surface by the activity of a metalloprotease. These results imply the existence of a putative secondary receptor for SV40 that might mediate SV40 entry. It is not yet clear whether class I molecules are active in transmitting the SV40 signal. Monoclonal antibodies against class I molecules also induce a signal in the SV40 host cells. However, the antibody-induced signal is mediated by mitogen-activated protein kinase (MAP kinase), whereas the SV40 signal is independent of MAP kinase.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10399061?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MHC class I molecules are enriched in caveolae but do not enter with simian virus 40.</style></title><secondary-title><style face="normal" font="default" size="100%">J Gen Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Gen. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1998 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">79 ( Pt 6)</style></volume><pages><style face="normal" font="default" size="100%">1469-77</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) binds to MHC class I molecules anywhere on the cell surface and then enters through caveolae. The fate of class I molecules after SV40 binding is not known. Sensitivity of 125I-surface-labelled class I molecules to papain cleavage was used to distinguish internalized class I molecules from class I molecules remaining at the cell surface. Whereas the caveolae-enriched membrane microdomain was found to also be enriched for class I molecules, no internalized papain-resistant 125I-surface-labelled class I molecules could be detected at any time in either control cells or in cells preadsorbed with saturating amounts of SV40. Instead, 125I-surface-labelled class I molecules, as well as preadsorbed 125I-labelled anti-class I antibodies, accumulated in the medium, coincident with the turnover of class I molecules at the cell surface. The class I heavy chains that accumulated in the medium were truncated and their release was specifically prevented by the metalloprotease inhibitor 1,10-phenanthroline. Thus, whereas class I molecules mediate SV40 binding, they do not appear to mediate SV40 entry.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9634090?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biol Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biol. Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Polyomavirus Transforming</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Coated Vesicles</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Organelles</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetradecanoylphorbol Acetate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">1825-34</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) entry leading to infection occurred only after the virus was at the cell surface for 1.5 to 2 h. SV40 infectious entry was not sensitive to cytosol acidification, a treatment that blocks endocytosis via clathrin-coated vesicles. Instead, SV40 infectious entry was blocked by treating cells with the phorbol ester PMA or nystatin, which selectively disrupts caveolae. In control experiments, transferrin internalization was sensitive to cytosol acidification but was not sensitive to PMA or nystatin. Also, absorbed transferrin entered cells within minutes. Finally, bound SV40 translocated to caveolin-enriched membrane complexes isolated by a Triton X-100 insolubility protocol. Treatment with nystatin did not impair SV40 binding but did block the partitioning of virus into the caveolin-enriched complexes.</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8930903?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Dangoria, N S</style></author><author><style face="normal" font="default" size="100%">Breau, W C</style></author><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Cishek, D M</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry.</style></title><secondary-title><style face="normal" font="default" size="100%">J Gen Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Gen. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Calmodulin-Dependent Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Cycle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Dual Specificity Phosphatase 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Genistein</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Immediate-Early Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoflavones</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitogen-Activated Protein Kinase 3</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitogen-Activated Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Naphthalenes</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphoprotein Phosphatases</style></keyword><keyword><style  face="normal" font="default" size="100%">Platelet-Derived Growth Factor</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Kinase C</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Phosphatase 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Tyrosine Phosphatases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein-Serine-Threonine Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-jun</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-myc</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-raf</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-sis</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Up-Regulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">77 ( Pt 9)</style></volume><pages><style face="normal" font="default" size="100%">2173-82</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) binding to growth-arrested cells activated an intracellular signalling pathway that induced the up-regulation of the primary response genes c-myc, c-jun and c-sis within 30 min and of JE within 90 min. The up-regulation of the primary response genes occurred in the presence of cycloheximide and when UV-inactivated SV40 was adsorbed to cells. SV40 binding did not activate Raf or mitogen-activated protein kinase (MAP/ERK1), or mobilize intracellular Ca2+. The SV40-induced up-regulation of c-myc and c-jun was blocked by the tyrosine kinase inhibitor, genistein, and by the protein kinase C (PKC) inhibitor, calphostin C, but not by expression of the MAP kinase-specific phosphatase, MKP-1. These results suggest that the SV40-induced signalling pathway includes the activities of a tyrosine kinase and a Ca(2+)-independent isoform of PKC, but not of Raf or MAP kinase. Finally, SV40 infectious entry into cells was specifically and reversibly blocked by genistein.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8811017?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author><author><style face="normal" font="default" size="100%">Anderson, H A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multiple stages of virus-receptor interactions as shown by simian virus 40.</style></title><secondary-title><style face="normal" font="default" size="100%">Adv Exp Med Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Adv. Exp. Med. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">408</style></volume><pages><style face="normal" font="default" size="100%">159-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8895788?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lafond, R E</style></author><author><style face="normal" font="default" size="100%">Giammalvo, J T</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Relationship between expression of epidermal growth factor and simian virus 40 T antigen in a line of transgenic mice.</style></title><secondary-title><style face="normal" font="default" size="100%">Transgenic Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Transgenic Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenocarcinoma</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Viral, Tumor</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Choroid Plexus</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">Epidermal Growth Factor</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Neoplastic</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney Tubules, Distal</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Transgenic</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Submandibular Gland</style></keyword><keyword><style  face="normal" font="default" size="100%">Submandibular Gland Neoplasms</style></keyword><keyword><style  face="normal" font="default" size="100%">Wnt Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Wnt1 Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Zebrafish Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">306-14</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The pattern of expression of the simian virus 40 (SV40) T antigen gene and resultant dysplasia were re-examined in a line of transgenic mice in which the T antigen gene was under the control of the SV40 early promoter. We found that T antigen expression in the kidney, and resulting dysplastic lesions, occurred exclusively in the distal convoluted tubules and the ascending limbs of Henle. Epidermal growth factor (EGF) expression in the kidney of normal mice was similarly immunolocalized. The correlation between high EGF immunoreactivity in normal mouse tissues and T antigen expression in the transgenic counterpart was also seen in the choroid plexus epithelium and in the submandibular glands of male mice. T antigen was not found in the submandibular gland of transgenic females. Similarly, EGF was only rarely detected in the normal female submandibular gland. In contrast to the correlation between T antigen expression in the transgenic mice and EGF expression in the corresponding tissues of the normal mice, within the dysplastic lesions of the transgenic mice EGF expression was severely diminished. Adenocarcinomas of the male submandibular gland from another line of transgenic mice that expresses the Int-1 transgene, showed similarly reduced levels of immunostaining for EGF. Thus, reduced expression of EGF might be a general feature of dysplasia and tumorigenesis in those tissues that normally express EGF.</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8589733?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Breau, W C</style></author><author><style face="normal" font="default" size="100%">Atwood, W J</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding, Competitive</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Flow Cytometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Precipitin Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Transfection</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1992</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1992 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">2037-45</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The class I molecules encoded by the major histocompatibility complex (MHC) present endogenously synthesized antigenic peptide fragments to cytotoxic T lymphocytes. We show here that these proteins are an essential component of the cell surface receptor for simian virus 40 (SV40). First, SV40 binding to cells can be blocked by two monoclonal antibodies against class I human lymphocyte antigen (HLA) proteins but not by monoclonal antibodies specific for other cell surface proteins. Second, SV40 does not bind to cells of two different human lymphoblastoid cell lines which do not express surface class I MHC proteins because of genetic defects in the beta 2-microglobulin gene in one line and in the HLA complex in the other. Transfection of these cell lines with cloned genes for beta 2-microglobulin and HLA-B8, respectively, restored expression of their surface class I MHC proteins and resulted in concomitant SV40 binding. Finally, SV40 binds to purified HLA proteins in vitro and selectively binds to class I MHC proteins in a cell surface extract.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1312619?dopt=Abstract</style></custom1></record></records></xml>